title: Nanobio interfaces: charge control of enzyme/inorganic interfaces for advanced biocatalysis.
abstract: Specific approaches to the rational design of nanobio interfaces for enzyme and protein binding to nanomaterials are vital for engineering advanced, functional nanobiomaterials for biocatalysis, sensing, and biomedical applications. This feature article presents an overview of our recent discoveries on structural, functional, and mechanistic details of how enzymes interact with inorganic nanomaterials and how they can be controlled in a systematic manner using α-Zr(IV)phosphate (α-ZrP) as a model system. The interactions of a number of enzymes having a wide array of surface charges, sizes, and functional groups are investigated. Interactions are carefully controlled to screen unfavorable repulsions and enhance favorable interactions for high affinity, structure retention, and activity preservation. In specific cases, catalytic activities and substrate selectivities are improved over those of the pristine enzymes, and two examples of high activity near the boiling point of water have been demonstrated. Isothermal titration calorimetric studies indicated that enzyme binding is coupled to ion sequestration or release to or from the nanobio interface, and binding is controlled in a rational manner. We learned that (1) bound enzyme stabilities are improved by lowering the entropy of the denatured state; (2) maximal loadings are obtained by matching charge footprints of the enzyme and the nanomaterial surface; (3) binding affinities are improved by ion sequestration at the nanobio interface; and (4) maximal enzyme structure retention is obtained by biophilizing the nanobio interface with protein glues. The chemical and physical manipulations of the nanobio interface are significant not only for understanding the complex behaviors of enzymes at biological interfaces but also for desiging better functional nanobiomaterials for a wide variety of practical applications.
authors.affiliation: Department of Chemistry and ‡Department of Molecular and Cell Biology, Institute of Material Science , 55 North Eagleville Road, Storrs, Connecticut 06226, United States.
authors.forename: Inoka K
authors.initials: IK
authors.lastname: Deshapriya
authors.forename: Challa V
authors.initials: CV
authors.lastname: Kumar
mesh_terms: D055162:Biocatalysis; D004795:Enzyme Stability; D004798:Enzymes / Q000737:chemistry* / Q000378:metabolism*; D007287:Inorganic Chemicals / Q000737:chemistry*; D049329:Nanostructures / Q000737:chemistry*; D036103:Nanotechnology / Q000379:methods*; D013816:Thermodynamics
chemical_list: D004798:Enzymes; D007287:Inorganic Chemicals